ArticleBiochimica et biophysica acta2013
Crystal structure-based exploration of the important role of Arg106 in the RNA-binding domain of human coronavirus OC43 nucleocapsid protein.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 53 citations in OpenAlex.
- A core network in the SARS-CoV-2 nucleocapsid NTD mediates structural integrity and selective RNA-binding.Nature communications · 2024Article
- Targeting protein-protein interaction interfaces with antiviral N protein inhibitor in SARS-CoV-2.Biophysical journal · 2024Article
- Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024Review
- Cell surface nucleocapsid protein expression: A betacoronavirus immunomodulatory strategy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cell Surface Nucleocapsid Protein Expression: A Betacoronavirus Immunomodulatory Strategy.bioRxiv : the preprint server for biology · 2023Article
- More or less deadly? A mathematical model that predicts SARS-CoV-2 evolutionary direction.Computers in biology and medicine · 2023Article
- Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein.Science bulletin · 2022Article
- Potential Coronaviral Inhibitors of the Nucleocapsid Protein Identified In Silico and In Vitro from a Large Natural Product Library.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain.Journal of the American Chemical Society · 2022Article
- Inhibitory efficacy of 2, 4-diacetylphloroglucinol against SARS-COV-2 proteins: in silico study.Biologia · 2022Article
- Comparing the Nucleocapsid Proteins of Human Coronaviruses: Structure, Immunoregulation, Vaccine, and Targeted Drug.Frontiers in molecular biosciences · 2022Review
- Targeting the N-Terminus Domain of the Coronavirus Nucleocapsid Protein Induces Abnormal Oligomerization via Allosteric Modulation.Frontiers in molecular biosciences · 2022Article
- Targeting the Interaction Between Spike Protein and Nucleocapsid Protein for Suppression and Detection of Human Coronavirus OC43.Frontiers in immunology · 2022Article
- Article
- Intracellular Life Cycle Kinetics of SARS-CoV-2 Predicted Using Mathematical Modelling.Viruses · 2021Article
- Microchip-based structure determination of low-molecular weight proteins using cryo-electron microscopy.Nanoscale · 2021Article
- Computational drug repurposing study of the RNA binding domain of SARS-CoV-2 nucleocapsid protein with antiviral agents.Biotechnology progress · 2021Article
- The SARS-Coronavirus Infection Cycle: A Survey of Viral Membrane Proteins, Their Functional Interactions and Pathogenesis.International journal of molecular sciences · 2021Review
- Review
- Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein.PLoS pathogens · 2020Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Human coronavirus OC43 (HCoV-OC43) is a causative agent of the common cold. The nucleocapsid (N) protein, which is a major structural protein of CoVs, binds to the viral RNA genome to form the virion core and results in the formation of the ribonucleoprotein (RNP) complex. We have solved the crystal structure of the N-terminal domain of HCoV-OC43 N protein (N-NTD) (residues 58 to 195) to a resolution of 2.0Å. The HCoV-OC43 N-NTD is a single domain protein composed of a five-stranded β-sheet core and a long extended loop, similar to that observed in the structures of N-NTDs from other coronaviruses. The positively charged loop of the HCoV-OC43 N-NTD contains a structurally well-conserved positively charged residue, R106. To assess the role of R106 in RNA binding, we undertook a series of site-directed mutagenesis experiments and docking simulations to characterize the interaction between R106 and RNA. The results show that R106 plays an important role in the interaction between the N protein and RNA. In addition, we showed that, in cells transfected with plasmids that encoded the mutant (R106A) N protein and infected with virus, the level of the matrix protein gene was decreased by 7-fold compared to cells that were transfected with the wild-type N protein. This finding suggests that R106, by enhancing binding of the N protein to viral RNA plays a critical role in the viral replication. The results also indicate that the strength of N protein/RNA interactions is critical for HCoV-OC43 replication.
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